5XW7
Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthase subunit C
Summary for 5XW7
| Entry DOI | 10.2210/pdb5xw7/pdb |
| Descriptor | Cellulose synthase subunit C (1 entity in total) |
| Functional Keywords | cellulose synthase, tetratrico peptide repeat, biosynthetic protein |
| Biological source | Enterobacter sp. CJF-002 |
| Total number of polymer chains | 5 |
| Total formula weight | 142770.15 |
| Authors | Nojima, S.,Kato, K.,Yao, M. (deposition date: 2017-06-29, release date: 2017-11-01, Last modification date: 2024-03-27) |
| Primary citation | Nojima, S.,Fujishima, A.,Kato, K.,Ohuchi, K.,Shimizu, N.,Yonezawa, K.,Tajima, K.,Yao, M. Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C Sci Rep, 7:13018-13018, 2017 Cited by PubMed Abstract: Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit considered to export BC to the extracellular matrix. It is predicted to have two domains: a tetratrico peptide repeat (TPR) domain and a β-barrelled outer membrane domain. Here we report the crystal structure of the N-terminal part of BcsC-TPR domain (Asp24-Arg272) derived from Enterobacter CJF-002. Unlike most TPR-containing proteins which have continuous TPR motifs, this structure has an extra α-helix between two clusters of TPR motifs. Five independent molecules in the crystal had three different conformations that varied at the hinge of the inserted α-helix. Such structural feature indicates that the inserted α-helix confers flexibility to the chain and changes the direction of the TPR super-helix, which was also suggested by structural analysis of BcsC-TPR (Asp24-Leu664) in solution by size exclusion chromatography-small-angle X-ray scattering. The flexibility at the α-helical hinge may play important role for exporting glucan chains. PubMed: 29026093DOI: 10.1038/s41598-017-12530-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.272 Å) |
Structure validation
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